SitesBLAST
Comparing WP_092482777.1 NCBI__GCF_900115975.1:WP_092482777.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2fuvA Phosphoglucomutase from salmonella typhimurium.
30% identity, 99% coverage: 4:493/496 of query aligns to 39:538/545 of 2fuvA
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
31% identity, 97% coverage: 6:484/496 of query aligns to 5:441/455 of 1wqaA
- active site: R11 (= R12), S101 (= S103), H102 (= H104), K111 (= K113), D243 (= D273), D245 (= D275), D247 (= D277), R248 (= R278), G330 (= G361), R340 (≠ K371)
- binding magnesium ion: S101 (= S103), D243 (= D273), D245 (= D275), D247 (= D277)
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
27% identity, 99% coverage: 2:493/496 of query aligns to 40:572/581 of P18159
- G162 (≠ A119) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ S215) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G361) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D372) mutation to N: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
Q9VUY9 Phosphoglucomutase 1; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
28% identity, 90% coverage: 36:482/496 of query aligns to 47:526/560 of Q9VUY9
- S116 (= S103) modified: Phosphoserine
- E351 (≠ A332) natural variant: E -> K
Sites not aligning to the query:
- 6 natural variant: E -> G
- 17 natural variant: K -> Q
- 28 natural variant: K -> N
- 36 natural variant: T -> M
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
25% identity, 94% coverage: 29:493/496 of query aligns to 54:547/573 of 6snoA
- active site: S130 (= S103), H131 (= H104), K143 (= K113), D301 (= D273), D303 (= D275), D305 (= D277), R306 (= R278), G393 (= G361)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S103), E389 (= E357), S391 (= S359), R514 (= R462), S516 (= S464), G517 (= G465), T518 (= T466), R526 (= R471)
- binding zinc ion: S130 (= S103), D301 (= D273), D303 (= D275), D305 (= D277)
Sites not aligning to the query:
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
25% identity, 94% coverage: 29:493/496 of query aligns to 54:540/566 of 6snqA
- active site: S130 (= S103), H131 (= H104), K143 (= K113), D301 (= D273), D303 (= D275), D305 (= D277), R306 (= R278), G393 (= G361)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S103), T370 (≠ V338), G371 (= G339), E389 (= E357), S391 (= S359), R512 (= R462), S514 (= S464), R519 (= R471)
- binding zinc ion: S130 (= S103), D301 (= D273), D303 (= D275), D305 (= D277)
Sites not aligning to the query:
P36871 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Homo sapiens (Human) (see 11 papers)
26% identity, 91% coverage: 45:493/496 of query aligns to 57:536/562 of P36871
- D62 (= D50) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ D56) to M: in allele PGM1*7+, allele PGM1*7-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type; dbSNP:rs200390982
- T115 (= T101) to A: in CDG1T; reduces mildly phosphoglucomutase activity; dbSNP:rs121918371
- S117 (= S103) active site, Phosphoserine intermediate; binding via phosphate groupe; modified: Phosphoserine
- G121 (≠ P107) to R: in CDG1T; there is 7% enzyme residual phosphoglucomutase activity; dbSNP:rs398122912
- R221 (≠ M208) to C: in allele PGM1*2+, allele PGM1*2-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type; dbSNP:rs1126728
- D263 (≠ E248) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D273) binding Mg(2+)
- D290 (= D275) binding Mg(2+)
- G291 (≠ A276) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D277) binding Mg(2+)
- G330 (= G310) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E358) to K: in CDG1T; decreases strongly solubility
- E388 (= E370) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
- Y420 (= Y402) to H: in allele PGM1*1-, allele PGM1*2-, allele PGM1*3- and allele PGM1*7-; phosphoglucomutase activity is similar to wild-type; dbSNP:rs11208257
- T467 (≠ V440) modified: Phosphothreonine; by PAK1
- L516 (≠ I472) to P: in CDG1T; decreases strongly solubility; dbSNP:rs587777401
Sites not aligning to the query:
- 19 T → A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- 38 N → Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- 41 Q → R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
5jn5A Crystal structure of the d263y missense variant of human pgm1 (see paper)
26% identity, 91% coverage: 45:493/496 of query aligns to 58:533/559 of 5jn5A
- active site: S118 (= S103), H119 (= H104), K131 (= K113), D289 (= D273), D291 (= D275), D293 (= D277), R294 (= R278), G381 (= G361), K390 (= K371)
- binding calcium ion: S118 (= S103), D289 (= D273), D291 (= D275), D293 (= D277)
Sites not aligning to the query:
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
26% identity, 87% coverage: 45:476/496 of query aligns to 57:520/562 of P00949
- S117 (= S103) active site, Phosphoserine intermediate; binding alpha-D-glucose 1,6-bisphosphate; binding via phosphate group; modified: Phosphoserine
- D288 (= D273) binding Mg(2+)
- D290 (= D275) binding Mg(2+)
- D292 (= D277) binding alpha-D-glucose 1,6-bisphosphate; binding Mg(2+)
- R293 (= R278) binding alpha-D-glucose 1,6-bisphosphate
- T357 (≠ V338) binding alpha-D-glucose 1,6-bisphosphate
- E376 (= E357) binding alpha-D-glucose 1,6-bisphosphate
- S378 (= S359) binding alpha-D-glucose 1,6-bisphosphate
- K389 (= K371) binding alpha-D-glucose 1,6-bisphosphate
Sites not aligning to the query:
- 23 binding alpha-D-glucose 1,6-bisphosphate
3pmgA Structure of rabbit muscle phosphoglucomutase at 2.4 angstroms resolution. Use of freezing point depressant and reduced temperature to enhance diffractivity (see paper)
26% identity, 87% coverage: 45:476/496 of query aligns to 56:519/561 of 3pmgA